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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6699938 [NCBI, ExPASy, EBI, Israel, Japan]
Mandart E.,
Kay A.,
Galibert F.;
"Nucleotide sequence of a cloned duck hepatitis B virus genome: comparison with woodchuck and human hepatitis B virus sequences.";
J. Virol. 49:782-792(1984).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 794-836.
PubMed=6328037 [NCBI, ExPASy, EBI, Israel, Japan]
Molnar-Kimber K.L.,
Summers J.W.,
Mason W.S.;
"Mapping of the cohesive overlap of duck hepatitis B virus DNA and of the site of initiation of reverse transcription.";
J. Virol. 51:181-191(1984).
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[3]
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ACTIVATION BY HOST HSC70 AND HSP40.
DOI=10.1074/jbc.M301069200; PubMed=12851401 [NCBI, ExPASy, EBI, Israel, Japan]
Beck J.,
Nassal M.;
"Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatitis B virus reverse transcriptase, an assumed Hsp90 client protein.";
J. Biol. Chem. 278:36128-36138(2003).
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[4]
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ACTIVATION BY HOST CHAPERONES.
DOI=10.1128/JVI.01196-07; PubMed=17913810 [NCBI, ExPASy, EBI, Israel, Japan]
Stahl M.,
Beck J.,
Nassal M.;
"Chaperones activate hepadnavirus reverse transcriptase by transiently exposing a C-proximal region in the terminal protein domain that contributes to epsilon RNA binding.";
J. Virol. 81:13354-13364(2007).
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[5]
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REVIEW.
PubMed=17206754 [NCBI, ExPASy, EBI, Israel, Japan]
Beck J.,
Nassal M.;
"Hepatitis B virus replication.";
World J. Gastroenterol. 13:48-64(2007).
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- FUNCTION: Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery (By similarity).
- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-phosphomonoester.
- ENZYME REGULATION: Activated by host HSP70 and HSP40 in vitro to be able to bind the epsilon loop of the pgRNA. Because deletion of the RNase H region renders the protein partly chaperone-independent, the chaperones may be needed indirectly to releive occlusion of the RNA-binding site by this domain.
- DOMAIN: Terminal protein domain (TP) is hepadnavirus-specific. Spacer domain is highly variable and separates the TP and RT domains. Polymerase/reverse-transcriptase domain (RT) and ribonuclease H domain (RH) are similar to retrovirus reverse transcriptase/RNase H (By similarity).
- DOMAIN: The polymerase/reverse transcriptase (RT) and ribonuclease H (RH) domains are structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the 'primer grip' region is thought to be involved in the positioning of the primer terminus for accommodating the incoming nucleotide. The RH domain stabilizes the association of RT with primer-template (By similarity).
- SIMILARITY: Belongs to the hepadnaviridae P protein family.
- SIMILARITY: Contains 1 reverse transcriptase domain.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 836 AA [This is the length of the unprocessed precursor] |
Molecular weight: 95276 Da [This is the MW of the unprocessed precursor] |
CRC64: FFEB57CFF549A4F4 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MQKLTRNHWI GLGDCFGGIT TVYCGEKLKL LTIFLVCVLG CQLLRNIEVE MPRPLKQSLD
70 80 90 100 110 120
QSRWLREAEK QLRVLENLVD SNLEEEKLKP QLSMGEDVQS PGKGEPLHPN VRAPLSHVVR
130 140 150 160 170 180
AATIDLPRLG NKLPARHHLG KLSGLYQMKG CTFNPEWKVP DISDTHFNLD VVNECPSRNW
190 200 210 220 230 240
KYLTPAKFWP KSISYFPVQV GVKPKYPDNV MQHESIVGKY LTRLYEAGIL YKRISKHLVT
250 260 270 280 290 300
FKGQPYNWEQ QHLVNQHHIY DGATSSKING RQTDRRRRNT VKPTCRKDDP KRDFDMVRQV
310 320 330 340 350 360
SNTRSRVRPC ANNGGDKHPP ESGSLACWGG KESRIIKSDS SRDSSAPVDS RGRPKSTRSF
370 380 390 400 410 420
SPLSRRKTTG NHHHSSVFPS SVEATTRGRS TPGKSVSPRD SSAIPVRTSG ASDKNSPLEE
430 440 450 460 470 480
ENVWYLRGNT SWPNRITGKL FLVDKNSRNT EEARLVVDFS QFSKGKNAMR FPRYWSPNLS
490 500 510 520 530 540
TLRRILPVGM PRISLDLSQA FYHLPLNPAS SSRLAVSDGQ RVYYFRKAPM GVGLSPFLLH
550 560 570 580 590 600
LFTTALGSEI SRRFNVWTFT YMDDFLLCHP NARHLNAISH AVCSFLQELG IRINFDKTTP
610 620 630 640 650 660
SPVNEIRFLG YQIDENFMKI EESRWKELRT VIKKIKVGEW YDWKCIQRFV GHLNFVLPFT
670 680 690 700 710 720
KGNIEMLKPM YAAITNQVNF SFSSSYRTLL YKLTMGVCKL RIKPKSSVPL PRVATDATPT
730 740 750 760 770 780
HGAISHITGG SAVFAFSKVR DIHVQELLMS CLAKIMIKPR CLLSDSTFVC HKRYQTLPWH
790 800 810 820 830
FAMLAKQLLK PIQLYFVPSK YNPADGPSRH KPPDWTAFPY TPLSKAIYIP HRLCGT
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P03162 in FASTA format |
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ExPASy Home page
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